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Science. 1997 Jun 27;276(5321):2042-5.

Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation.

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1
Vollum Institute, Oregon Health Sciences University, Portland, OR 97201, USA.

Abstract

Long-term potentiation (LTP), a cellular model of learning and memory, requires calcium-dependent protein kinases. Induction of LTP increased the phosphorus-32 labeling of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors (AMPA-Rs), which mediate rapid excitatory synaptic transmission. This AMPA-R phosphorylation appeared to be catalyzed by Ca2+- and calmodulin-dependent protein kinase II (CaM-KII): (i) it correlated with the activation and autophosphorylation of CaM-KII, (ii) it was blocked by the CaM-KII inhibitor KN-62, and (iii) its phosphorus-32 peptide map was the same as that of GluR1 coexpressed with activated CaM-KII in HEK-293 cells. This covalent modulation of AMPA-Rs in LTP provides a postsynaptic molecular mechanism for synaptic plasticity.

PMID:
9197267
DOI:
10.1126/science.276.5321.2042
[Indexed for MEDLINE]
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